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Database: PDB
Entry: 5G53
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Original site: 5G53 
HEADER    SIGNALING PROTEIN                       19-MAY-16   5G53              
TITLE     STRUCTURE OF THE ADENOSINE A2A RECEPTOR BOUND TO AN ENGINEERED G      
TITLE    2 PROTEIN                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ADENOSINE RECEPTOR A2A;                                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES;                                                       
COMPND   6 OTHER_DETAILS: THE CONSTRUCT WAS TRUNCATED AFTER RESIDUE 308 OF THE  
COMPND   7 A2A SEQUENCE, BUT HAS A 6 RESIDUE SEQUENCE THAT INCLUDES THE TEV     
COMPND   8 CLEAVAGE SEQUENCE (ENLYFQ) AT THE C- TERMINUS;                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: ENGINEERED DOMAIN OF HUMAN G ALPHA S LONG ISOFORM;         
COMPND  11 CHAIN: C, D;                                                         
COMPND  12 FRAGMENT: RAS DOMAIN, RESIDUES 26-60 AND 847-1037;                   
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MUTATION: YES;                                                       
COMPND  15 OTHER_DETAILS: DELETIONS 1-25,65-203,255-264 INSERTION GGSGGSGG      
COMPND  16 LINKING RESIDUES 64 AND 204                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 TISSUE: BRAIN;                                                       
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS FLASHBAC ULTRA;           
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PBACPAK8;                                 
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 TISSUE: BRAIN;                                                       
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VARIANT: CODONPLUS-RIL;                            
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: MULTI-COPY PLASMID;                   
SOURCE  21 EXPRESSION_SYSTEM_VECTOR: PET15B                                     
KEYWDS    SIGNALING PROTEIN, G PROTEIN COUPLED RECEPTOR, ADENOSINE RECEPTOR,    
KEYWDS   2 SEVEN-HELIX RECEPTOR, INTEGRAL MEMBRANE PROTEIN, GPCR, ENGINEERED G  
KEYWDS   3 PROTEIN, GPCR-G PROTEIN COMPLEX, MINI-GS                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.CARPENTER,R.NEHME,T.WARNE,A.G.W.LESLIE,C.G.TATE                     
REVDAT   4   08-MAR-17 5G53    1       JRNL                                     
REVDAT   3   24-AUG-16 5G53    1       JRNL                                     
REVDAT   2   10-AUG-16 5G53    1       JRNL                                     
REVDAT   1   03-AUG-16 5G53    0                                                
JRNL        AUTH   B.CARPENTER,R.NEHME,T.WARNE,A.G.W.LESLIE,C.G.TATE            
JRNL        TITL   STRUCTURE OF THE ADENOSINE A2A RECEPTOR BOUND TO AN          
JRNL        TITL 2 ENGINEERED G PROTEIN                                         
JRNL        REF    NATURE                        V. 536   104 2016              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   27462812                                                     
JRNL        DOI    10.1038/NATURE18966                                          
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   G.LEBON,T.WARNE,P.C.EDWARDS,K.BENNETT,C.J.LANGMEAD,          
REMARK   1  AUTH 2 A.G.W.LESLIE,C.G.TATE                                        
REMARK   1  TITL   AGONIST-BOUND ADENOSINE A2A RECEPTOR STRUCTURES REVEAL       
REMARK   1  TITL 2 COMMON FEATURES OF GPCR ACTIVATION                           
REMARK   1  REF    NATURE                        V. 474   521 2011              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1  PMID   21593763                                                     
REMARK   1  DOI    10.1038/NATURE10136                                          
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   B.CARPENTER,C.G.TATE                                         
REMARK   1  TITL   ENGINEERING A MINIMAL G PROTEIN TO FACILITATE                
REMARK   1  TITL 2 CRYSTALLISATION OF G PROTEIN-COUPLED RECEPTORS IN THEIR      
REMARK   1  TITL 3 ACTIVE CONFORMATION.                                         
REMARK   1  REF    PROTEIN ENG. DES. SEL.        V.  29   583 2016              
REMARK   1  REFN                   ESSN 1741-0134                               
REMARK   1  PMID   27672048                                                     
REMARK   1  DOI    10.1093/PROTEIN/GZW049                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0144                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 91.89                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 19788                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.285                           
REMARK   3   R VALUE            (WORKING SET) : 0.284                           
REMARK   3   FREE R VALUE                     : 0.315                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1089                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.49                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 903                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 56.48                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4080                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 64                           
REMARK   3   BIN FREE R VALUE                    : 0.3820                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7247                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 112                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 76.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.78000                                             
REMARK   3    B22 (A**2) : -3.88000                                             
REMARK   3    B33 (A**2) : 5.66000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.690         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.697         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 46.428        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.828                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.811                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7546 ; 0.008 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  7116 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10315 ; 1.149 ; 1.958       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 16166 ; 0.923 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   937 ; 5.295 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   291 ;35.502 ;23.024       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1092 ;16.014 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    33 ;13.261 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1234 ; 0.115 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8458 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1845 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3781 ; 3.020 ; 7.920       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3780 ; 3.021 ; 7.919       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4707 ; 5.207 ;11.876       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3765 ; 2.219 ; 8.045       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  5608 ; 3.942 ;12.013       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. U VALUES REFINED INDIVIDUALLY SIDE CHAINS WITHOUT        
REMARK   3  CLEAR ELECTRON DENSITY HAVE BEEN TRUNCATED BACK TO CBETA.           
REMARK   4                                                                      
REMARK   4 5G53 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-MAY-16.                  
REMARK 100 THE PDBE ID CODE IS EBI-66872.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-APR-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.872900                           
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : KB MIRRORS                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20898                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.300                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.6                               
REMARK 200  DATA REDUNDANCY                : 2.600                              
REMARK 200  R MERGE                    (I) : 0.17000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 3.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 78.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.75000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRIES 2YDV, 3SN6                               
REMARK 200                                                                      
REMARK 200 REMARK: THE RAS DOMAIN FROM ENTRY 3SN6 WAS USED FOR MOLECULAR        
REMARK 200  REPLACEMENT                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NAOAC PH 5.5, 10% PEG 2000 (IN     
REMARK 280  THE PRESENCE OF CHS); OR 0.1 M NAOAC PH 5.7, 9.5% PEG 2000 MME      
REMARK 280  (IN THE ABSENCE OF CHS)                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       45.31600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       80.65200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.90700            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       80.65200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       45.31600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.90700            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4140 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22500 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.2 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     ILE A     3                                                      
REMARK 465     MET A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     GLY A   147                                                      
REMARK 465     GLN A   148                                                      
REMARK 465     PRO A   149                                                      
REMARK 465     LYS A   150                                                      
REMARK 465     GLU A   151                                                      
REMARK 465     GLY A   152                                                      
REMARK 465     LYS A   153                                                      
REMARK 465     ALA A   154                                                      
REMARK 465     HIS A   155                                                      
REMARK 465     SER A   156                                                      
REMARK 465     GLN A   157                                                      
REMARK 465     GLY A   158                                                      
REMARK 465     GLU A   212                                                      
REMARK 465     SER A   213                                                      
REMARK 465     GLN A   214                                                      
REMARK 465     PRO A   215                                                      
REMARK 465     LEU A   216                                                      
REMARK 465     PRO A   217                                                      
REMARK 465     GLY A   218                                                      
REMARK 465     GLU A   219                                                      
REMARK 465     ARG A   220                                                      
REMARK 465     ALA A   221                                                      
REMARK 465     ARG A   222                                                      
REMARK 465     SER A   223                                                      
REMARK 465     PHE A   313                                                      
REMARK 465     GLN A   314                                                      
REMARK 465     MET B     1                                                      
REMARK 465     PRO B     2                                                      
REMARK 465     ILE B     3                                                      
REMARK 465     MET B     4                                                      
REMARK 465     GLY B     5                                                      
REMARK 465     LEU B   208                                                      
REMARK 465     LYS B   209                                                      
REMARK 465     GLN B   210                                                      
REMARK 465     MET B   211                                                      
REMARK 465     GLU B   212                                                      
REMARK 465     SER B   213                                                      
REMARK 465     GLN B   214                                                      
REMARK 465     PRO B   215                                                      
REMARK 465     LEU B   216                                                      
REMARK 465     PRO B   217                                                      
REMARK 465     GLY B   218                                                      
REMARK 465     GLU B   219                                                      
REMARK 465     ARG B   220                                                      
REMARK 465     ALA B   221                                                      
REMARK 465     ARG B   222                                                      
REMARK 465     SER B   223                                                      
REMARK 465     HIS B   306                                                      
REMARK 465     VAL B   307                                                      
REMARK 465     LEU B   308                                                      
REMARK 465     GLU B   309                                                      
REMARK 465     ASN B   310                                                      
REMARK 465     LEU B   311                                                      
REMARK 465     TYR B   312                                                      
REMARK 465     PHE B   313                                                      
REMARK 465     GLN B   314                                                      
REMARK 465     GLY C    25                                                      
REMARK 465     ILE C    26                                                      
REMARK 465     GLU C    27                                                      
REMARK 465     LYS C    28                                                      
REMARK 465     GLN C    29                                                      
REMARK 465     LEU C    30                                                      
REMARK 465     GLN C    31                                                      
REMARK 465     LYS C    32                                                      
REMARK 465     ASP C    33                                                      
REMARK 465     LYS C    34                                                      
REMARK 465     GLN C    35                                                      
REMARK 465     VAL C    36                                                      
REMARK 465     TYR C    37                                                      
REMARK 465     ARG C    38                                                      
REMARK 465     ALA C    39                                                      
REMARK 465     ILE C   193                                                      
REMARK 465     TYR C   194                                                      
REMARK 465     HIS C   195                                                      
REMARK 465     GLY C   196                                                      
REMARK 465     GLY C   197                                                      
REMARK 465     SER C   198                                                      
REMARK 465     GLY C   199                                                      
REMARK 465     GLY C   200                                                      
REMARK 465     SER C   201                                                      
REMARK 465     GLY C   202                                                      
REMARK 465     GLY C   203                                                      
REMARK 465     THR C   204                                                      
REMARK 465     SER C   205                                                      
REMARK 465     GLY C   206                                                      
REMARK 465     ILE C   207                                                      
REMARK 465     ALA C   366                                                      
REMARK 465     VAL C   367                                                      
REMARK 465     ASP C   368                                                      
REMARK 465     GLY D    25                                                      
REMARK 465     ILE D    26                                                      
REMARK 465     GLU D    27                                                      
REMARK 465     LYS D    28                                                      
REMARK 465     GLN D    29                                                      
REMARK 465     LEU D    30                                                      
REMARK 465     GLN D    31                                                      
REMARK 465     LYS D    32                                                      
REMARK 465     ASP D    33                                                      
REMARK 465     LYS D    34                                                      
REMARK 465     GLN D    35                                                      
REMARK 465     VAL D    36                                                      
REMARK 465     TYR D    37                                                      
REMARK 465     ARG D    38                                                      
REMARK 465     ILE D   193                                                      
REMARK 465     TYR D   194                                                      
REMARK 465     HIS D   195                                                      
REMARK 465     GLY D   196                                                      
REMARK 465     GLY D   197                                                      
REMARK 465     SER D   198                                                      
REMARK 465     GLY D   199                                                      
REMARK 465     GLY D   200                                                      
REMARK 465     SER D   201                                                      
REMARK 465     GLY D   202                                                      
REMARK 465     GLY D   203                                                      
REMARK 465     THR D   204                                                      
REMARK 465     SER D   205                                                      
REMARK 465     GLY D   206                                                      
REMARK 465     ILE D   207                                                      
REMARK 465     GLY D   225                                                      
REMARK 465     GLY D   226                                                      
REMARK 465     GLN D   227                                                      
REMARK 465     ARG D   228                                                      
REMARK 465     ASP D   229                                                      
REMARK 465     GLU D   230                                                      
REMARK 465     ARG D   231                                                      
REMARK 465     ARG D   232                                                      
REMARK 465     LYS D   233                                                      
REMARK 465     TRP D   234                                                      
REMARK 465     ILE D   235                                                      
REMARK 465     GLN D   236                                                      
REMARK 465     CYS D   237                                                      
REMARK 465     PHE D   238                                                      
REMARK 465     LEU D   394                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 107    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 161    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 199    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 209    CG   CD   CE   NZ                                   
REMARK 470     GLU A 228    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 293    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 294    CG   CD   OE1  OE2                                  
REMARK 470     GLN B  38    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 102    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 107    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 122    CG   CD   CE   NZ                                   
REMARK 470     GLU B 151    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 161    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 199    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 206    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 226    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 227    CG   CD   CE   NZ                                   
REMARK 470     GLU B 228    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 261    CG   OD1  OD2                                       
REMARK 470     ARG B 291    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 293    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C  58    CG   CD   CE   NZ                                   
REMARK 470     GLN C  59    CG   CD   OE1  NE2                                  
REMARK 470     MET C  60    CG   SD   CE                                        
REMARK 470     ARG C  61    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 209    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 215    CG   OD1  OD2                                       
REMARK 470     LYS C 216    CG   CD   CE   NZ                                   
REMARK 470     ARG C 228    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP C 229    CG   OD1  OD2                                       
REMARK 470     LYS C 233    CG   CD   CE   NZ                                   
REMARK 470     GLU C 268    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 280    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 283    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 299    CG   CD   OE1  OE2                                  
REMARK 470     LEU C 302    CG   CD1  CD2                                       
REMARK 470     LYS C 305    CG   CD   CE   NZ                                   
REMARK 470     LYS C 307    CG   CD   CE   NZ                                   
REMARK 470     GLU C 322    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 330    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 333    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP C 354    CG   OD1  OD2                                       
REMARK 470     ARG C 356    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     CYS C 365    SG                                                  
REMARK 470     THR C 369    OG1  CG2                                            
REMARK 470     GLU C 370    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 373    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 385    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 389    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN C 390    CG   CD   OE1  NE2                                  
REMARK 470     GLN D  59    CG   CD   OE1  NE2                                  
REMARK 470     ARG D  61    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 209    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 211    CG   CD   CE   NZ                                   
REMARK 470     LYS D 216    CG   CD   CE   NZ                                   
REMARK 470     HIS D 220    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP D 240    CG   OD1  OD2                                       
REMARK 470     LYS D 274    CG   CD   CE   NZ                                   
REMARK 470     ARG D 280    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TRP D 281    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP D 281    CZ3  CH2                                            
REMARK 470     LYS D 300    CG   CD   CE   NZ                                   
REMARK 470     LYS D 305    CG   CD   CE   NZ                                   
REMARK 470     LYS D 307    CG   CD   CE   NZ                                   
REMARK 470     GLU D 309    CG   CD   OE1  OE2                                  
REMARK 470     ASP D 310    CG   OD1  OD2                                       
REMARK 470     ARG D 317    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 322    CG   CD   OE1  OE2                                  
REMARK 470     ASP D 323    CG   OD1  OD2                                       
REMARK 470     ARG D 333    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 336    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 347    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 356    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     CYS D 365    SG                                                  
REMARK 470     VAL D 367    CG1  CG2                                            
REMARK 470     ASP D 368    CG   OD1  OD2                                       
REMARK 470     THR D 369    OG1  CG2                                            
REMARK 470     GLU D 370    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 385    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN D 390    CG   CD   OE1  NE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A 180      -60.53   -105.08                                   
REMARK 500    GLN B 148       69.79   -119.98                                   
REMARK 500    PHE B 180      -60.63   -105.21                                   
REMARK 500    VAL C 224       53.92   -155.08                                   
REMARK 500    GLN C 227      -13.07     91.10                                   
REMARK 500    GLU C 230       -3.57     78.44                                   
REMARK 500    PHE C 238      -90.22    114.97                                   
REMARK 500    ASN C 239      -39.77     74.27                                   
REMARK 500    ASP C 240       38.03    -98.05                                   
REMARK 500    THR C 325       73.69   -118.44                                   
REMARK 500    ASP D 240       41.96    -96.36                                   
REMARK 500    THR D 325       73.02   -118.81                                   
REMARK 500    ALA D 366      -54.04     66.70                                   
REMARK 500    ASP D 368      126.44    -38.46                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NEC A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SOG A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SOG A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NEC B 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP C 400                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 A2A RECEPTOR. THE CONSTRUCT WAS TRUNCATED AFTER RESIDUE              
REMARK 999 308 OF THE A2A SEQUENCE.  REMOVAL OF GLYCOSYLATION SITE BY           
REMARK 999 MUTATION N154A. AT C-TERMINUS,THERE IS A TEV CLEAVAGE                
REMARK 999 SEQUENCE ENLYFQ                                                      
REMARK 999 ENGINEERED G ALPHA S. DELETIONS 1-25, 65-203, 255-264.               
REMARK 999 MUTATIONS G49D, E50N, L63Y, A249D, S252D, L272D, I372A,              
REMARK 999 V375I. INSERTION GGSGGSGG LINKING RESIDUES 64 AND 204.               
REMARK 999 ADDITIONAL G RESIDUE AT N TERMINUS FROM TEV CLEAVAGE SITE.           
DBREF  5G53 A    1   308  UNP    P29274   AA2AR_HUMAN      1    308             
DBREF  5G53 B    1   308  UNP    P29274   AA2AR_HUMAN      1    308             
DBREF  5G53 C   26    60  UNP    P63092   GNAS2_HUMAN     26     60             
DBREF  5G53 C  204   394  UNP    Q5JWF2   GNAS1_HUMAN    847   1037             
DBREF  5G53 D   26    60  UNP    P63092   GNAS2_HUMAN     26     60             
DBREF  5G53 D  204   394  UNP    Q5JWF2   GNAS1_HUMAN    847   1037             
SEQADV 5G53 ALA A  154  UNP  P29274    ASN   154 ENGINEERED MUTATION            
SEQADV 5G53 GLU A  309  UNP  P29274              EXPRESSION TAG                 
SEQADV 5G53 ASN A  310  UNP  P29274              EXPRESSION TAG                 
SEQADV 5G53 LEU A  311  UNP  P29274              EXPRESSION TAG                 
SEQADV 5G53 TYR A  312  UNP  P29274              EXPRESSION TAG                 
SEQADV 5G53 PHE A  313  UNP  P29274              EXPRESSION TAG                 
SEQADV 5G53 GLN A  314  UNP  P29274              EXPRESSION TAG                 
SEQADV 5G53 ALA B  154  UNP  P29274    ASN   154 ENGINEERED MUTATION            
SEQADV 5G53 GLU B  309  UNP  P29274              EXPRESSION TAG                 
SEQADV 5G53 ASN B  310  UNP  P29274              EXPRESSION TAG                 
SEQADV 5G53 LEU B  311  UNP  P29274              EXPRESSION TAG                 
SEQADV 5G53 TYR B  312  UNP  P29274              EXPRESSION TAG                 
SEQADV 5G53 PHE B  313  UNP  P29274              EXPRESSION TAG                 
SEQADV 5G53 GLN B  314  UNP  P29274              EXPRESSION TAG                 
SEQADV 5G53 GLY C   25  UNP  P63092              EXPRESSION TAG                 
SEQADV 5G53 ASP C   49  UNP  P63092    GLY    49 ENGINEERED MUTATION            
SEQADV 5G53 ASN C   50  UNP  P63092    GLU    50 ENGINEERED MUTATION            
SEQADV 5G53 ARG C   61  UNP  P63092              LINKER                         
SEQADV 5G53 ILE C  193  UNP  P63092              LINKER                         
SEQADV 5G53 TYR C  194  UNP  P63092              LINKER                         
SEQADV 5G53 HIS C  195  UNP  P63092              LINKER                         
SEQADV 5G53 GLY C  196  UNP  P63092              LINKER                         
SEQADV 5G53 GLY C  197  UNP  P63092              LINKER                         
SEQADV 5G53 SER C  198  UNP  P63092              LINKER                         
SEQADV 5G53 GLY C  199  UNP  P63092              LINKER                         
SEQADV 5G53 GLY C  200  UNP  P63092              LINKER                         
SEQADV 5G53 SER C  201  UNP  P63092              LINKER                         
SEQADV 5G53 GLY C  202  UNP  P63092              LINKER                         
SEQADV 5G53 GLY C  203  UNP  P63092              LINKER                         
SEQADV 5G53 ASP C  249  UNP  Q5JWF2    ALA   892 ENGINEERED MUTATION            
SEQADV 5G53 ASP C  252  UNP  Q5JWF2    SER   895 ENGINEERED MUTATION            
SEQADV 5G53     C       UNP  Q5JWF2    ASN   897 DELETION                       
SEQADV 5G53     C       UNP  Q5JWF2    MET   898 DELETION                       
SEQADV 5G53     C       UNP  Q5JWF2    VAL   899 DELETION                       
SEQADV 5G53     C       UNP  Q5JWF2    ILE   900 DELETION                       
SEQADV 5G53     C       UNP  Q5JWF2    ARG   901 DELETION                       
SEQADV 5G53     C       UNP  Q5JWF2    GLU   902 DELETION                       
SEQADV 5G53     C       UNP  Q5JWF2    ASP   903 DELETION                       
SEQADV 5G53     C       UNP  Q5JWF2    ASN   904 DELETION                       
SEQADV 5G53     C       UNP  Q5JWF2    GLN   905 DELETION                       
SEQADV 5G53     C       UNP  Q5JWF2    THR   906 DELETION                       
SEQADV 5G53 ASP C  272  UNP  Q5JWF2    LEU   915 ENGINEERED MUTATION            
SEQADV 5G53 ALA C  372  UNP  Q5JWF2    ILE  1015 ENGINEERED MUTATION            
SEQADV 5G53 ILE C  375  UNP  Q5JWF2    VAL  1018 ENGINEERED MUTATION            
SEQADV 5G53 GLY D   25  UNP  P63092              EXPRESSION TAG                 
SEQADV 5G53 ASP D   49  UNP  P63092    GLY    49 ENGINEERED MUTATION            
SEQADV 5G53 ASN D   50  UNP  P63092    GLU    50 ENGINEERED MUTATION            
SEQADV 5G53 ARG D   61  UNP  P63092              LINKER                         
SEQADV 5G53 ILE D  193  UNP  P63092              LINKER                         
SEQADV 5G53 TYR D  194  UNP  P63092              LINKER                         
SEQADV 5G53 HIS D  195  UNP  P63092              LINKER                         
SEQADV 5G53 GLY D  196  UNP  P63092              LINKER                         
SEQADV 5G53 GLY D  197  UNP  P63092              LINKER                         
SEQADV 5G53 SER D  198  UNP  P63092              LINKER                         
SEQADV 5G53 GLY D  199  UNP  P63092              LINKER                         
SEQADV 5G53 GLY D  200  UNP  P63092              LINKER                         
SEQADV 5G53 SER D  201  UNP  P63092              LINKER                         
SEQADV 5G53 GLY D  202  UNP  P63092              LINKER                         
SEQADV 5G53 GLY D  203  UNP  P63092              LINKER                         
SEQADV 5G53 ASP D  249  UNP  Q5JWF2    ALA   892 ENGINEERED MUTATION            
SEQADV 5G53 ASP D  252  UNP  Q5JWF2    SER   895 ENGINEERED MUTATION            
SEQADV 5G53     D       UNP  Q5JWF2    ASN   897 DELETION                       
SEQADV 5G53     D       UNP  Q5JWF2    MET   898 DELETION                       
SEQADV 5G53     D       UNP  Q5JWF2    VAL   899 DELETION                       
SEQADV 5G53     D       UNP  Q5JWF2    ILE   900 DELETION                       
SEQADV 5G53     D       UNP  Q5JWF2    ARG   901 DELETION                       
SEQADV 5G53     D       UNP  Q5JWF2    GLU   902 DELETION                       
SEQADV 5G53     D       UNP  Q5JWF2    ASP   903 DELETION                       
SEQADV 5G53     D       UNP  Q5JWF2    ASN   904 DELETION                       
SEQADV 5G53     D       UNP  Q5JWF2    GLN   905 DELETION                       
SEQADV 5G53     D       UNP  Q5JWF2    THR   906 DELETION                       
SEQADV 5G53 ASP D  272  UNP  Q5JWF2    LEU   915 ENGINEERED MUTATION            
SEQADV 5G53 ALA D  372  UNP  Q5JWF2    ILE  1015 ENGINEERED MUTATION            
SEQADV 5G53 ILE D  375  UNP  Q5JWF2    VAL  1018 ENGINEERED MUTATION            
SEQRES   1 A  314  MET PRO ILE MET GLY SER SER VAL TYR ILE THR VAL GLU          
SEQRES   2 A  314  LEU ALA ILE ALA VAL LEU ALA ILE LEU GLY ASN VAL LEU          
SEQRES   3 A  314  VAL CYS TRP ALA VAL TRP LEU ASN SER ASN LEU GLN ASN          
SEQRES   4 A  314  VAL THR ASN TYR PHE VAL VAL SER LEU ALA ALA ALA ASP          
SEQRES   5 A  314  ILE ALA VAL GLY VAL LEU ALA ILE PRO PHE ALA ILE THR          
SEQRES   6 A  314  ILE SER THR GLY PHE CYS ALA ALA CYS HIS GLY CYS LEU          
SEQRES   7 A  314  PHE ILE ALA CYS PHE VAL LEU VAL LEU THR GLN SER SER          
SEQRES   8 A  314  ILE PHE SER LEU LEU ALA ILE ALA ILE ASP ARG TYR ILE          
SEQRES   9 A  314  ALA ILE ARG ILE PRO LEU ARG TYR ASN GLY LEU VAL THR          
SEQRES  10 A  314  GLY THR ARG ALA LYS GLY ILE ILE ALA ILE CYS TRP VAL          
SEQRES  11 A  314  LEU SER PHE ALA ILE GLY LEU THR PRO MET LEU GLY TRP          
SEQRES  12 A  314  ASN ASN CYS GLY GLN PRO LYS GLU GLY LYS ALA HIS SER          
SEQRES  13 A  314  GLN GLY CYS GLY GLU GLY GLN VAL ALA CYS LEU PHE GLU          
SEQRES  14 A  314  ASP VAL VAL PRO MET ASN TYR MET VAL TYR PHE ASN PHE          
SEQRES  15 A  314  PHE ALA CYS VAL LEU VAL PRO LEU LEU LEU MET LEU GLY          
SEQRES  16 A  314  VAL TYR LEU ARG ILE PHE LEU ALA ALA ARG ARG GLN LEU          
SEQRES  17 A  314  LYS GLN MET GLU SER GLN PRO LEU PRO GLY GLU ARG ALA          
SEQRES  18 A  314  ARG SER THR LEU GLN LYS GLU VAL HIS ALA ALA LYS SER          
SEQRES  19 A  314  LEU ALA ILE ILE VAL GLY LEU PHE ALA LEU CYS TRP LEU          
SEQRES  20 A  314  PRO LEU HIS ILE ILE ASN CYS PHE THR PHE PHE CYS PRO          
SEQRES  21 A  314  ASP CYS SER HIS ALA PRO LEU TRP LEU MET TYR LEU ALA          
SEQRES  22 A  314  ILE VAL LEU SER HIS THR ASN SER VAL VAL ASN PRO PHE          
SEQRES  23 A  314  ILE TYR ALA TYR ARG ILE ARG GLU PHE ARG GLN THR PHE          
SEQRES  24 A  314  ARG LYS ILE ILE ARG SER HIS VAL LEU GLU ASN LEU TYR          
SEQRES  25 A  314  PHE GLN                                                      
SEQRES   1 B  314  MET PRO ILE MET GLY SER SER VAL TYR ILE THR VAL GLU          
SEQRES   2 B  314  LEU ALA ILE ALA VAL LEU ALA ILE LEU GLY ASN VAL LEU          
SEQRES   3 B  314  VAL CYS TRP ALA VAL TRP LEU ASN SER ASN LEU GLN ASN          
SEQRES   4 B  314  VAL THR ASN TYR PHE VAL VAL SER LEU ALA ALA ALA ASP          
SEQRES   5 B  314  ILE ALA VAL GLY VAL LEU ALA ILE PRO PHE ALA ILE THR          
SEQRES   6 B  314  ILE SER THR GLY PHE CYS ALA ALA CYS HIS GLY CYS LEU          
SEQRES   7 B  314  PHE ILE ALA CYS PHE VAL LEU VAL LEU THR GLN SER SER          
SEQRES   8 B  314  ILE PHE SER LEU LEU ALA ILE ALA ILE ASP ARG TYR ILE          
SEQRES   9 B  314  ALA ILE ARG ILE PRO LEU ARG TYR ASN GLY LEU VAL THR          
SEQRES  10 B  314  GLY THR ARG ALA LYS GLY ILE ILE ALA ILE CYS TRP VAL          
SEQRES  11 B  314  LEU SER PHE ALA ILE GLY LEU THR PRO MET LEU GLY TRP          
SEQRES  12 B  314  ASN ASN CYS GLY GLN PRO LYS GLU GLY LYS ALA HIS SER          
SEQRES  13 B  314  GLN GLY CYS GLY GLU GLY GLN VAL ALA CYS LEU PHE GLU          
SEQRES  14 B  314  ASP VAL VAL PRO MET ASN TYR MET VAL TYR PHE ASN PHE          
SEQRES  15 B  314  PHE ALA CYS VAL LEU VAL PRO LEU LEU LEU MET LEU GLY          
SEQRES  16 B  314  VAL TYR LEU ARG ILE PHE LEU ALA ALA ARG ARG GLN LEU          
SEQRES  17 B  314  LYS GLN MET GLU SER GLN PRO LEU PRO GLY GLU ARG ALA          
SEQRES  18 B  314  ARG SER THR LEU GLN LYS GLU VAL HIS ALA ALA LYS SER          
SEQRES  19 B  314  LEU ALA ILE ILE VAL GLY LEU PHE ALA LEU CYS TRP LEU          
SEQRES  20 B  314  PRO LEU HIS ILE ILE ASN CYS PHE THR PHE PHE CYS PRO          
SEQRES  21 B  314  ASP CYS SER HIS ALA PRO LEU TRP LEU MET TYR LEU ALA          
SEQRES  22 B  314  ILE VAL LEU SER HIS THR ASN SER VAL VAL ASN PRO PHE          
SEQRES  23 B  314  ILE TYR ALA TYR ARG ILE ARG GLU PHE ARG GLN THR PHE          
SEQRES  24 B  314  ARG LYS ILE ILE ARG SER HIS VAL LEU GLU ASN LEU TYR          
SEQRES  25 B  314  PHE GLN                                                      
SEQRES   1 C  229  GLY ILE GLU LYS GLN LEU GLN LYS ASP LYS GLN VAL TYR          
SEQRES   2 C  229  ARG ALA THR HIS ARG LEU LEU LEU LEU GLY ALA ASP ASN          
SEQRES   3 C  229  SER GLY LYS SER THR ILE VAL LYS GLN MET ARG ILE TYR          
SEQRES   4 C  229  HIS GLY GLY SER GLY GLY SER GLY GLY THR SER GLY ILE          
SEQRES   5 C  229  PHE GLU THR LYS PHE GLN VAL ASP LYS VAL ASN PHE HIS          
SEQRES   6 C  229  MET PHE ASP VAL GLY GLY GLN ARG ASP GLU ARG ARG LYS          
SEQRES   7 C  229  TRP ILE GLN CYS PHE ASN ASP VAL THR ALA ILE ILE PHE          
SEQRES   8 C  229  VAL VAL ASP SER SER ASP TYR ASN ARG LEU GLN GLU ALA          
SEQRES   9 C  229  LEU ASN ASP PHE LYS SER ILE TRP ASN ASN ARG TRP LEU          
SEQRES  10 C  229  ARG THR ILE SER VAL ILE LEU PHE LEU ASN LYS GLN ASP          
SEQRES  11 C  229  LEU LEU ALA GLU LYS VAL LEU ALA GLY LYS SER LYS ILE          
SEQRES  12 C  229  GLU ASP TYR PHE PRO GLU PHE ALA ARG TYR THR THR PRO          
SEQRES  13 C  229  GLU ASP ALA THR PRO GLU PRO GLY GLU ASP PRO ARG VAL          
SEQRES  14 C  229  THR ARG ALA LYS TYR PHE ILE ARG ASP GLU PHE LEU ARG          
SEQRES  15 C  229  ILE SER THR ALA SER GLY ASP GLY ARG HIS TYR CYS TYR          
SEQRES  16 C  229  PRO HIS PHE THR CYS ALA VAL ASP THR GLU ASN ALA ARG          
SEQRES  17 C  229  ARG ILE PHE ASN ASP CYS ARG ASP ILE ILE GLN ARG MET          
SEQRES  18 C  229  HIS LEU ARG GLN TYR GLU LEU LEU                              
SEQRES   1 D  229  GLY ILE GLU LYS GLN LEU GLN LYS ASP LYS GLN VAL TYR          
SEQRES   2 D  229  ARG ALA THR HIS ARG LEU LEU LEU LEU GLY ALA ASP ASN          
SEQRES   3 D  229  SER GLY LYS SER THR ILE VAL LYS GLN MET ARG ILE TYR          
SEQRES   4 D  229  HIS GLY GLY SER GLY GLY SER GLY GLY THR SER GLY ILE          
SEQRES   5 D  229  PHE GLU THR LYS PHE GLN VAL ASP LYS VAL ASN PHE HIS          
SEQRES   6 D  229  MET PHE ASP VAL GLY GLY GLN ARG ASP GLU ARG ARG LYS          
SEQRES   7 D  229  TRP ILE GLN CYS PHE ASN ASP VAL THR ALA ILE ILE PHE          
SEQRES   8 D  229  VAL VAL ASP SER SER ASP TYR ASN ARG LEU GLN GLU ALA          
SEQRES   9 D  229  LEU ASN ASP PHE LYS SER ILE TRP ASN ASN ARG TRP LEU          
SEQRES  10 D  229  ARG THR ILE SER VAL ILE LEU PHE LEU ASN LYS GLN ASP          
SEQRES  11 D  229  LEU LEU ALA GLU LYS VAL LEU ALA GLY LYS SER LYS ILE          
SEQRES  12 D  229  GLU ASP TYR PHE PRO GLU PHE ALA ARG TYR THR THR PRO          
SEQRES  13 D  229  GLU ASP ALA THR PRO GLU PRO GLY GLU ASP PRO ARG VAL          
SEQRES  14 D  229  THR ARG ALA LYS TYR PHE ILE ARG ASP GLU PHE LEU ARG          
SEQRES  15 D  229  ILE SER THR ALA SER GLY ASP GLY ARG HIS TYR CYS TYR          
SEQRES  16 D  229  PRO HIS PHE THR CYS ALA VAL ASP THR GLU ASN ALA ARG          
SEQRES  17 D  229  ARG ILE PHE ASN ASP CYS ARG ASP ILE ILE GLN ARG MET          
SEQRES  18 D  229  HIS LEU ARG GLN TYR GLU LEU LEU                              
HET    NEC  A 400      22                                                       
HET    SOG  A 501      20                                                       
HET    SOG  A 502      20                                                       
HET    NEC  B 400      22                                                       
HET    GDP  C 400      28                                                       
HETNAM     NEC N-ETHYL-5'-CARBOXAMIDO ADENOSINE                                 
HETNAM     SOG 2-HYDROXYMETHYL-6-OCTYLSULFANYL-TETRAHYDRO-PYRAN-3,4,5-          
HETNAM   2 SOG  TRIOL                                                           
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
HETSYN     SOG 1-S-OCTYL-BETA-D-THIOGLUCOSIDE                                   
FORMUL   5  NEC    2(C12 H16 N6 O4)                                             
FORMUL   6  SOG    2(C14 H28 O5 S)                                              
FORMUL   9  GDP    C10 H15 N5 O11 P2                                            
HELIX    1   1 SER A    6  ASN A   34  1                                  29    
HELIX    2   2 VAL A   40  LEU A   58  1                                  19    
HELIX    3   3 LEU A   58  THR A   68  1                                  11    
HELIX    4   4 ALA A   73  ILE A  108  1                                  36    
HELIX    5   5 ARG A  111  VAL A  116  1                                   6    
HELIX    6   6 THR A  117  LEU A  137  1                                  21    
HELIX    7   7 THR A  138  GLY A  142  5                                   5    
HELIX    8   8 LEU A  167  VAL A  172  1                                   6    
HELIX    9   9 PRO A  173  PHE A  180  1                                   8    
HELIX   10  10 PHE A  180  VAL A  186  1                                   7    
HELIX   11  11 VAL A  186  MET A  211  1                                  26    
HELIX   12  12 THR A  224  CYS A  259  1                                  36    
HELIX   13  13 PRO A  266  THR A  279  1                                  14    
HELIX   14  14 THR A  279  TYR A  290  1                                  12    
HELIX   15  15 ILE A  292  LEU A  311  1                                  20    
HELIX   16  16 SER B    6  ASN B   34  1                                  29    
HELIX   17  17 VAL B   40  LEU B   58  1                                  19    
HELIX   18  18 LEU B   58  THR B   68  1                                  11    
HELIX   19  19 ALA B   73  ILE B  108  1                                  36    
HELIX   20  20 ARG B  111  VAL B  116  1                                   6    
HELIX   21  21 THR B  117  LEU B  137  1                                  21    
HELIX   22  22 THR B  138  GLY B  142  5                                   5    
HELIX   23  23 LYS B  150  GLN B  157  1                                   8    
HELIX   24  24 LEU B  167  VAL B  172  1                                   6    
HELIX   25  25 PRO B  173  PHE B  180  1                                   8    
HELIX   26  26 PHE B  180  VAL B  186  1                                   7    
HELIX   27  27 VAL B  186  GLN B  207  1                                  22    
HELIX   28  28 THR B  224  CYS B  259  1                                  36    
HELIX   29  29 PRO B  266  THR B  279  1                                  14    
HELIX   30  30 THR B  279  TYR B  290  1                                  12    
HELIX   31  31 ILE B  292  SER B  305  1                                  14    
HELIX   32  32 GLY C   52  ARG C   61  1                                  10    
HELIX   33  33 GLU C  230  GLN C  236  1                                   7    
HELIX   34  34 ASN C  254  ASN C  279  1                                  16    
HELIX   35  35 LYS C  293  GLY C  304  1                                  12    
HELIX   36  36 LYS C  307  PHE C  312  1                                   6    
HELIX   37  37 PRO C  313  TYR C  318  5                                   6    
HELIX   38  38 ASP C  331  SER C  352  1                                  22    
HELIX   39  39 GLU C  370  TYR C  391  1                                  22    
HELIX   40  40 GLY D   52  ARG D   61  1                                  10    
HELIX   41  41 ASN D  254  ASN D  279  1                                  16    
HELIX   42  42 LYS D  293  GLY D  304  1                                  12    
HELIX   43  43 LYS D  307  PHE D  312  1                                   6    
HELIX   44  44 PRO D  313  TYR D  318  5                                   6    
HELIX   45  45 ASP D  331  SER D  352  1                                  22    
HELIX   46  46 GLU D  370  TYR D  391  1                                  22    
SHEET    1  AA 2 CYS A  71  ALA A  72  0                                        
SHEET    2  AA 2 VAL A 164  ALA A 165 -1  O  VAL A 164   N  ALA A  72           
SHEET    1  BA 2 CYS B  71  ALA B  72  0                                        
SHEET    2  BA 2 VAL B 164  ALA B 165 -1  O  VAL B 164   N  ALA B  72           
SHEET    1  CA 6 GLU C 209  VAL C 214  0                                        
SHEET    2  CA 6 VAL C 217  ASP C 223 -1  O  VAL C 217   N  VAL C 214           
SHEET    3  CA 6 HIS C  41  GLY C  47  1  O  HIS C  41   N  HIS C 220           
SHEET    4  CA 6 ALA C 243  ASP C 249  1  O  ALA C 243   N  LEU C  44           
SHEET    5  CA 6 SER C 286  ASN C 292  1  O  SER C 286   N  ILE C 244           
SHEET    6  CA 6 CYS C 359  PHE C 363  1  O  TYR C 360   N  LEU C 289           
SHEET    1  DA 6 GLU D 209  VAL D 214  0                                        
SHEET    2  DA 6 VAL D 217  ASP D 223 -1  O  VAL D 217   N  VAL D 214           
SHEET    3  DA 6 HIS D  41  GLY D  47  1  O  HIS D  41   N  HIS D 220           
SHEET    4  DA 6 ALA D 243  ASP D 249  1  O  ALA D 243   N  LEU D  44           
SHEET    5  DA 6 VAL D 287  ASN D 292  1  O  ILE D 288   N  PHE D 246           
SHEET    6  DA 6 CYS D 359  PHE D 363  1  O  TYR D 360   N  LEU D 289           
SSBOND   1 CYS A   71    CYS A  159                          1555   1555  2.04  
SSBOND   2 CYS A   74    CYS A  146                          1555   1555  2.04  
SSBOND   3 CYS A   77    CYS A  166                          1555   1555  2.03  
SSBOND   4 CYS A  259    CYS A  262                          1555   1555  2.03  
SSBOND   5 CYS B   71    CYS B  159                          1555   1555  2.05  
SSBOND   6 CYS B   74    CYS B  146                          1555   1555  2.04  
SSBOND   7 CYS B   77    CYS B  166                          1555   1555  2.03  
SSBOND   8 CYS B  259    CYS B  262                          1555   1555  2.02  
SITE     1 AC1 15 VAL A  84  LEU A  85  THR A  88  GLN A  89                    
SITE     2 AC1 15 PHE A 168  GLU A 169  MET A 177  ASN A 181                    
SITE     3 AC1 15 TRP A 246  HIS A 250  ASN A 253  MET A 270                    
SITE     4 AC1 15 ILE A 274  SER A 277  HIS A 278                               
SITE     1 AC2  7 LEU A  26  PRO A 285  PHE A 286  TYR A 290                    
SITE     2 AC2  7 ARG A 296  PHE A 299  ARG A 300                               
SITE     1 AC3  2 THR A 119  ALA A 126                                          
SITE     1 AC4 15 VAL B  84  LEU B  85  THR B  88  GLN B  89                    
SITE     2 AC4 15 PHE B 168  GLU B 169  MET B 177  ASN B 181                    
SITE     3 AC4 15 TRP B 246  HIS B 250  ASN B 253  MET B 270                    
SITE     4 AC4 15 ILE B 274  SER B 277  HIS B 278                               
SITE     1 AC5 12 ALA C  48  ASP C  49  ASN C  50  SER C  51                    
SITE     2 AC5 12 GLY C  52  LYS C  53  SER C  54  THR C  55                    
SITE     3 AC5 12 ASN C 292  LYS C 293  ASP C 295  CYS C 365                    
CRYST1   90.632  111.814  161.304  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011034  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008943  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006199        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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